Comparison of the ANTH domain of CALM to the ENTH domain of epsin1 (see details)

Overexpression of AP180 C-terminus leads to the inhibition of all clathrin budding pathways and a tubulation of AP1 positive compartments (see details).

Major questions still to be answered:
A. Does AP180 control the size of a clathrin-coated vesicle?
B. Does AP180 function independently of AP2 adaptors to recruit clathrin?

Focus on our publications related to this protein

Ford, M.G.J., Pearse, B., Higgins, M., Vallis, Y., Owen, D., Gibson, A., Hopkins, C.R., Evans, P.R. and McMahon, H.T. (2001) Simultaneous binding of PtdIns(4,5)P2 and clathrin by AP180 causes nucleation of clathrin lattices on
membranes. Science. 291, 1051-1055 (abstract),(pdf). (Also see cover and highlight in same issue)
It was clear to us when we published this paper that the ANTH domain of AP180 was distinct from the ENTH domain of epsin. We discuss this issue further in our Epsin web pages, but in this paper we chose to call this domain AP180-N, and it was not until we had solved the structure of the ENTH domain bound to PtdIns(4,5)P2 that we found the mode of lipid binding was different, and we classified AP180-like proteins as having ANTH domains. Mao et al also published the structure of Drosophila LAP ANTH domain in Cell in the same year (abstract) (pdf).